ArticlePloS one2024
The gag-like gene RTL8 antagonizes PEG10-mediated virus like particles.
Article in PloS one, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Engineering human PEG10-based nanoparticles for RNA self-packaging, delivery and cancer therapy.Nature communications · 2026Article
- Review
- Probing the molecular determinants of Ty1 retrotransposon restriction specificity in yeast.PLoS genetics · 2025Article
- UBQLN2 in neurodegenerative disease: mechanistic insights and emerging therapeutic potential.Biochemical Society transactions · 2025Review
- Endogenous retrovirus-like proteins recruit UBQLN2 to stress granules and shape their functional biology.Science advances · 2025Article
- Roles of PEG10 in cancer and neurodegenerative disorder (Review).Oncology reports · 2025Review
- The Diverse Evolutionary Histories of Domesticated Metaviral Capsid Genes in Mammals.Molecular biology and evolution · 2024Article
- Precise Therapy Using the Selective Endogenous Encapsidation for Cellular Delivery Vector System.Pharmaceutics · 2024Review
- The diverse evolutionary histories of domesticated metaviral capsid genes in mammals.bioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
PEG10 is a retroelement-derived Mart-family gene that is necessary for placentation and has been implicated in neurological disease. PEG10 resembles both retrotransposon and retroviral proteins and forms virus-like particles (VLPs) that can be purified using iodixanol ultracentrifugation. It is hypothesized that formation of VLPs is crucial to the biological roles of PEG10 in reproduction and neurological health. Here, we describe the regulation of PEG10 VLP formation and release in human cells with a role for the related Mart gene RTL8. RTL8 resembles a truncated form of PEG10 that shares homology with the N-terminal gag-like capsid domain. Alone, RTL8 is unable to form VLPs, but was incorporated into PEG10-derived particles. RTL8 co-expression decreased the abundance of PEG10 VLPs and increased intracellular levels of PEG10, suggesting a model where RTL8 inhibits PEG10 VLP formation or release. Consistent with this model, RTL8 bound to the N-terminal domain of PEG10 capsid, and modulation of RTL8 influenced PEG10-derived VLP abundance in naturally producing cells. RTL8 is broadly expressed in many of the same tissues as PEG10, including in human brain. Taken together, these results describe a novel antagonistic relationship between two human retroelement-derived genes and have implications for our understanding of PEG10 biology and disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.